O09130 · NF2IP_MOUSE
- ProteinNFATC2-interacting protein
- GeneNfatc2ip
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids412 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
In T-helper 2 (Th2) cells, regulates the magnitude of NFAT-driven transcription of a specific subset of cytokine genes, including IL3, IL4, IL5 and IL13, but not IL2. Recruits PRMT1 to the IL4 promoter; this leads to enhancement of histone H4 'Arg-3'-methylation and facilitates subsequent histone acetylation at the IL4 locus, thus promotes robust cytokine expression. Down-regulates formation of poly-SUMO chains by UBE2I/UBC9.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Biological Process | positive regulation of transcription by RNA polymerase II |
Names & Taxonomy
Protein names
- Recommended nameNFATC2-interacting protein
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionO09130
- Secondary accessions
Proteomes
Organism-specific databases
Phenotypes & Variants
Disruption phenotype
Mutant mice are born at the expected Mendelian ratio and appear healthy and viable. No alteration in thymic T-cell populations, T-cell proliferation, or peripheral lymphocyte development. Inefficient type-2 antiparasitic immune response to the intestinal nematode Trichinella spiralis due to impaired IL4 and IL13 cytokine production by Th2 cells.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 32 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000281009 | 1-412 | NFATC2-interacting protein | |||
Sequence: MAEPLRGRGPRSRGGRGARRARGARGRCPRARQSPARLIPDTVLVDLVSDSDEEVLEVADPVEVPVARLPAPAKPEQDSDSDSEGAAEGPAGAPRTLVRRRRRRLLDPGEAPVVPVYSGKVQSSLNLIPDNSSLLKLCPSEPEDEADLTNSGSSPSEDDALPSGSPWRKKLRKKCEKEEKKMEEFPDQDISPLPQPSSRNKSRKHTEALQKLREVNKRLQDLRSCLSPKQHQSPALQSTDDEVVLVEGPVLPQSSRLFTLKIRCRADLVRLPVRMSEPLQNVVDHMANHLGVSPNRILLLFGESELSPTATPSTLKLGVADIIDCVVLASSSEATETSQELRLRVQGKEKHQMLEISLSPDSPLKVLMSHYEEAMGLSGHKLSFFFDGTKLSGKELPADLGLESGDLIEVWG | ||||||
Modified residue | 49 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 51 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 79 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 81 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 83 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 118 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 120 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 191 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 197 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 307 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 309 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 311 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 362 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 383 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Methylation at the N-terminus by PRMT1 modulates interaction with the NFAT complex and results in augmented cytokine production.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highest level detected in spleen, thymus and testis.
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, coiled coil, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-38 | Disordered | ||||
Sequence: MAEPLRGRGPRSRGGRGARRARGARGRCPRARQSPARL | ||||||
Compositional bias | 12-27 | Basic residues | ||||
Sequence: SRGGRGARRARGARGR | ||||||
Region | 58-115 | Disordered | ||||
Sequence: VADPVEVPVARLPAPAKPEQDSDSDSEGAAEGPAGAPRTLVRRRRRRLLDPGEAPVVP | ||||||
Region | 136-206 | Disordered | ||||
Sequence: KLCPSEPEDEADLTNSGSSPSEDDALPSGSPWRKKLRKKCEKEEKKMEEFPDQDISPLPQPSSRNKSRKHT | ||||||
Compositional bias | 146-160 | Polar residues | ||||
Sequence: ADLTNSGSSPSEDDA | ||||||
Compositional bias | 163-187 | Basic and acidic residues | ||||
Sequence: SGSPWRKKLRKKCEKEEKKMEEFPD | ||||||
Coiled coil | 168-227 | |||||
Sequence: RKKLRKKCEKEEKKMEEFPDQDISPLPQPSSRNKSRKHTEALQKLREVNKRLQDLRSCLS | ||||||
Domain | 341-412 | Ubiquitin-like | ||||
Sequence: LRLRVQGKEKHQMLEISLSPDSPLKVLMSHYEEAMGLSGHKLSFFFDGTKLSGKELPADLGLESGDLIEVWG |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length412
- Mass (Da)45,121
- Last updated1997-07-01 v1
- ChecksumDD58FE5C7055C186
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0U1RNY9 | A0A0U1RNY9_MOUSE | Nfatc2ip | 110 |
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 2 | in Ref. 2; BAC26788 | ||||
Sequence: A → G | ||||||
Compositional bias | 12-27 | Basic residues | ||||
Sequence: SRGGRGARRARGARGR | ||||||
Compositional bias | 146-160 | Polar residues | ||||
Sequence: ADLTNSGSSPSEDDA | ||||||
Compositional bias | 163-187 | Basic and acidic residues | ||||
Sequence: SGSPWRKKLRKKCEKEEKKMEEFPD | ||||||
Sequence conflict | 200 | in Ref. 2; BAC26788 | ||||
Sequence: N → D | ||||||
Sequence conflict | 390-391 | in Ref. 2; BAB24331 | ||||
Sequence: KL → NS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U76759 EMBL· GenBank· DDBJ | AAC52963.1 EMBL· GenBank· DDBJ | mRNA | ||
AK005947 EMBL· GenBank· DDBJ | BAB24331.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AK030107 EMBL· GenBank· DDBJ | BAC26788.1 EMBL· GenBank· DDBJ | mRNA | ||
BC113761 EMBL· GenBank· DDBJ | AAI13762.1 EMBL· GenBank· DDBJ | mRNA |